Swiss-Prot entry
ID AKT1_ARATH STANDARD; PRT; 857 AA.
AC Q38998; Q38797; Q84MA7;
DT 29-MAR-2004 (Rel. 43, Created)
DT 29-MAR-2004 (Rel. 43, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Potassium channel AKT1.
GN Name=AKT1; OrderedLocusNames=At2g26650; ORFNames=F18A8.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Landsberg erecta;
RX MEDLINE=92263099; PubMed=1585180 [NCBI, ExPASy, EBI, Israel, Japan];
RA Sentenac H., Bonneaud N., Minet M., Lacroute F., Salmon J.-M.,
RA Gaymard F., Grignon C.;
RT "Cloning and expression in yeast of a plant potassium ion transport
RT system.";
RL Science 256:663-665(1992).
RN [2]
RP SEQUENCE REVISION.
RA Sentenac H.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX MEDLINE=96145506; PubMed=8555458 [NCBI, ExPASy, EBI, Israel, Japan];
RA Basset M., Conejero G., Lepetit M., Fourcroy P., Sentenac H.;
RT "Organization and expression of the gene coding for the potassium
RT transport system AKT1 of Arabidopsis thaliana.";
RL Plant Mol. Biol. 29:947-958(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=20083487; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:761-768(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-857.
RC STRAIN=cv. Columbia;
RX MEDLINE=22954850; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP TISSUE SPECIFICITY.
RX MEDLINE=96417815; PubMed=8820606 [NCBI, ExPASy, EBI, Israel, Japan];
RA Lagarde D., Basset M., Lepetit M., Conejero G., Gaymard F., Astruc S.,
RA Grignon C.;
RT "Tissue-specific expression of Arabidopsis AKT1 gene is consistent
RT with a role in K+ nutrition.";
RL Plant J. 9:195-203(1996).
RN [7]
RP SUBUNIT.
RX PubMed=9218788 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1093/emboj/16.12.3455;
RA Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I.;
RT "Tetramerization of the AKT1 plant potassium channel involves its C-
RT terminal cytoplasmic domain.";
RL EMBO J. 16:3455-3463(1997).
RN [8]
RP FUNCTION.
RX PubMed=9572739 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1126/science.280.5365.918;
RA Hirsch R.E., Lewis B.D., Spalding E.P., Sussman M.R.;
RT "A role for the AKT1 potassium channel in plant nutrition.";
RL Science 280:918-921(1998).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX MEDLINE=21392307; PubMed=11500563 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A.,
RA Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
RN [10]
RP FUNCTION, INTERACTIONS WITH AKT2 AND KAT3, AND INDUCTION.
RX PubMed=12678562 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1023/A:1022597102282;
RA Pilot G., Gaymard F., Mouline K., Cherel I., Sentenac H.;
RT "Regulated expression of Arabidopsis shaker K(+) channel genes
RT involved in K(+) uptake and distribution in the plant.";
RL Plant Mol. Biol. 51:773-787(2003).
CC -!- FUNCTION: Highly selective inward-rectifying potassium channel
CC that could mediate potassium uptake by plant roots. Assuming
CC opened or closed conformations in response to the voltage
CC difference across the membrane, the channel is activated by
CC hyperpolarization. May interact with the cytoskeleton or with
CC regulatory proteins.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. Possible
CC heteromultimer with AKT2 or KAT3.
CC -!- SUBCELLULAR LOCATION: Integral membrane protein.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the peripheral
CC cell layers of root mature including root cortex and root hairs.
CC Detected also, at a lower level, in the mesophyll of the leaves
CC and at restricted sites corresponding to hydathodes and guard
CC cells.
CC -!- INDUCTION: In roots, strongly reduced after 2,4-
CC dichlorophenoxyacetic acid (2,4-D) treatment and weakly reduced
CC after benzyladenine (BA) treatment. In shoots, strongly reduced
CC after abscisic acid (ABA) treatment and induced after
CC benzyladenine (BA) treatment.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids. The
CC pore-forming region H5 is enclosed by the transmembrane segments
CC S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD
CC signature motif which seems to be involved in potassium
CC selectivity.
CC -!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
CC present in the C-terminal part is likely to be important for
CC tetramerization.
CC -!- SIMILARITY: Belongs to the potassium channel (TC 1.A.1.4) family.
CC -!- SIMILARITY: Contains 6 ANK repeats.
CC -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC -!- SIMILARITY: Contains 1 KHA domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; X62907; CAA44693.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U06745; AAA96810.1; -; Unassigned_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AC003105; AAB95299.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BT006442; AAP21250.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; S23606; S23606.
DR PIR; S62694; S62694.
DR HSSP; P55271; 1D9S. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR GeneFarm; 2792; 266.
DR InterPro; IPR002110; ANK.
DR InterPro; IPR000595; cNMP_binding.
DR InterPro; IPR003938; EAG_ELK_ERG.
DR InterPro; IPR005821; Ion_trans.
DR InterPro; IPR001622; K+channel_pore.
DR InterPro; IPR005820; M+channel_nlg.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00023; Ank; 4.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00100; cNMP; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR CMR; Q38998.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR BLOCKS; Q38998.
DR ProtoNet; Q38998.
DR ProtoMap; Q38998.
DR PRESAGE; Q38998.
DR DIP; Q38998.
DR ModBase; Q38998.
DR TAIR; At2g26650.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW ANK repeat; Ion transport; Ionic channel; Potassium;
KW Potassium channel; Potassium transport; Repeat; Transmembrane;
KW Transport; Voltage-gated channel.
FT TOPO_DOM 1 61 Cytoplasmic (Potential).
FT TRANSMEM 62 82 Segment S1 (Potential).
FT TRANSMEM 91 111 Segment S2 (Potential).
FT TOPO_DOM 112 134 Cytoplasmic (Potential).
FT TRANSMEM 135 155 Segment S3 (Potential).
FT TRANSMEM 159 179 Segment S4 (Potential).
FT TOPO_DOM 180 193 Cytoplasmic (Potential).
FT TRANSMEM 194 214 Segment S5 (Potential).
FT TRANSMEM 266 286 Segment S6 (Potential).
FT TOPO_DOM 287 857 Cytoplasmic (Potential).
FT REPEAT 515 546 ANK 1.
FT REPEAT 550 579 ANK 2.
FT REPEAT 583 612 ANK 3.
FT REPEAT 614 643 ANK 4.
FT REPEAT 647 676 ANK 5.
FT REPEAT 680 709 ANK 6.
FT DOMAIN 801 857 KHA.
FT NP_BIND 372 493 cNMP.
FT REGION 242 261 Segment H5 (pore-forming, in membrane)
FT (Potential).
SQ SEQUENCE 857 AA; 96990 MW; 28E1622BA3505F4C CRC64;
MRGGALLCGQ VQDEIEQLSR ESSHFSLSTG ILPSLGARSN RRVKLRRFVV SPYDHKYRIW
EAFLVVLVVY TAWVSPFEFG FLRKPRPPLS ITDNIVNAFF AIDIIMTFFV GYLDKSTYLI
VDDRKQIAFK YLRSWFLLDL VSTIPSEAAM RISSQSYGLF NMLRLWRLRR VGALFARLEK
DRNFNYFWVR CAKLVCVTLF AVHCAACFYY LIAARNSNPA KTWIGANVAN FLEESLWMRY
VTSMYWSITT LTTVGYGDLH PVNTKEMIFD IFYMLFNLGL TAYLIGNMTN LVVHGTSRTR
NFRDTIQAAS NFAHRNHLPP RLQDQMLAHL CLKYRTDSEG LQQQETLDAL PKAIRSSISH
FLFYSLMDKV YLFRGVSNDL LFQLVSEMKA EYFPPKEDVI LQNEAPTDFY ILVNGTADLV
DVDTGTESIV REVKAGDIIG EIGVLCYRPQ LFTVRTKRLC QLLRMNRTTF LNIIQANVGD
GTIIMNNLLQ HLKEMNDPVM TNVLLEIENM LARGKMDLPL NLCFAAIRED DLLLHQLLKR
GLDPNESDNN GRTPLHIAAS KGTLNCVLLL LEYHADPNCR DAEGSVPLWE AMVEGHEKVV
KVLLEHGSTI DAGDVGHFAC TAAEQGNLKL LKEIVLHGGD VTRPRATGTS ALHTAVCEEN
IEMVKYLLEQ GADVNKQDMH GWTPRDLAEQ QGHEDIKALF REKLHERRVH IETSSSVPIL
KTGIRFLGRF TSEPNIRPAS REVSFRIRET RARRKTNNFD NSLFGILANQ SVPKNGLATV
DEGRTGNPVR VTISCAEKDD IAGKLVLLPG SFKELLELGS NKFGIVATKV MNKDNNAEID
DVDVIRDGDH LIFATDS
//